The Collectables: Year in Bioanalysis UPDATE
Webinar: Quantification of proteins in complex biological samples by LC–MS/MS: an Editorial update with Rainer Bischoff
Rainer Bischoff
Analytical Biochemistry, Department of Pharmacy, University of Groningen, Antonius Deusinglaan 1, 9713 AV Groningen, Te Netherlands
r.p.h.bischoff@
rug.nl
Te use of LC–MS/MS in quantitative bioanalysis of therapeutic proteins in complex biological samples has expanded in the last year. Notably, the advent of combining high-resolution mass spectrometry (HRMS) with LC has opened new possibilities, both at the peptide level after protein digestion and at the protein level itself. While still challenging, more and more groups in academia and in industry have published results on combining HPLC separations at the protein level with HRMS. It is fair to say that most of these applications fall within the area of product characterization [1–5], but first attempts at translating them to the bioanalysis of proteins have appeared [6,7].
Tere is also renewed interest in developing LC stationary phases and mobile phase compositions for the online coupling of protein LC to mass spectrometry [1,2,4]. Tis is due to the fact that the community would like to get a better view of protein heterogeneity, as this may affect efficacy, immunogenicity and toxicity. Recent attempts at mimicking in vivo protein biotransformation under controlled in vitro conditions [3,8] show that this aspect of therapeutic protein monitoring is gaining momentum based on earlier studies [9].
References
1 Chen B, Lin Z, Alpert AJ et al. Online hydrophobic interaction chromatography–mass spectrometry for the analysis of intact monoclonal antibodies. Anal. Chem. 90(12), 7135–7138 (2018).
2
Füssl F, Cook K, Scheffler K, Farrell A, Mittermayr S, Bones J. Charge variant analysis of monoclonal antibodies using direct coupled ph gradient cation exchange chromatography to high-resolution native mass spectrometry. Anal. Chem. 90(70), 4669–4676 (2018).
3 Nowak C, Tiwari A, Liu H. Asparagine deamidation in a complementarity determining region of a recombinant monoclonal antibody in complex with antigen. Anal. Chem. 90(11), 6998–7003 (2018).
4
Szabo Z, Thayer JR, Reusch D et al. High performance anion exchange and hydrophilic interaction liquid chromatography approaches for comprehensive mass spectrometry-based characterization of the n-glycome of a recombinant human erythropoietin. J. Proteome Res. 17(4), 1559–1574 (2018).
5 Tassi M, De Vos J, Chatterjee, S, Sobott F,
Bones J, Eeltink S. Advances in native high- performance liquid chromatography and
intact mass spectrometry for the characterization of biopharmaceutical products. J. Sep. Sci. 41(1),
125–144 (2018). 6
Jin W, Burton L, Moore I. LC-HRMS quantitation of intact antibody drug conjugate trastuzumab emtansine from rat plasma. Bioanalysis 10(11), 851–862 (2018).
7 Vasicek LA, Spellman DS, Hsieh S et al. Quantitation of a therapeutic antibody in serum using intact sequential affinity capture, trypsin digestion, and LC-MS/MS. Anal. Chem. 90(1), 866–871
(2018).
8 Yang N, Tang Q, Hu P, Lewis MJ. Use of in vitro systems to model in vivo degradation of therapeutic monoclonal antibodies. Anal. Chem. doi:10.1021/acs.
analchem.8b00183 (2018) (Epub ahead of print).
9 Bults P, Bischoff R, Bakker H, Gietema JA, van de Merbel NC. LC-MS/MS-based monitoring of in vivo protein biotransformation: quantitative determination of trastuzumab and its deamidation products in human plasma. Anal. Chem. 88(3), 1871–1877 (2015).
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